Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/80363
DC Field | Value | Language |
---|---|---|
dc.contributor | Department of Applied Biology and Chemical Technology | - |
dc.creator | Lin, P | - |
dc.creator | Liu, D | - |
dc.creator | Wei, W | - |
dc.creator | Guo, J | - |
dc.creator | Ke, S | - |
dc.creator | Zeng, X | - |
dc.creator | Chen, S | - |
dc.date.accessioned | 2019-02-20T01:14:16Z | - |
dc.date.available | 2019-02-20T01:14:16Z | - |
dc.identifier.issn | 1388-2481 | en_US |
dc.identifier.uri | http://hdl.handle.net/10397/80363 | - |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.rights | © 2018 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY license (http://creativecommons.org/licenses/BY-NC-ND/4.0/) | en_US |
dc.rights | The following publication: Lin, P., Liu, D., Wei, W., Guo, J., Ke, S., Zeng, X., & Chen, S. (2018). A novel protein binding strategy for energy-transfer-based photoelectrochemical detection of enzymatic activity of botulinum neurotoxin A. Electrochemistry Communications, 97, 114-118 is available at https://doi.org/10.1016/j.elecom.2018.11.004 | en_US |
dc.subject | Botulinum neurotoxin A | en_US |
dc.subject | CdS QDs | en_US |
dc.subject | Energy transfer | en_US |
dc.subject | Exciton–plasmon interaction | en_US |
dc.subject | Photoelectrochemical detection | en_US |
dc.title | A novel protein binding strategy for energy-transfer-based photoelectrochemical detection of enzymatic activity of Botulinum Neurotoxin A | en_US |
dc.type | Journal/Magazine Article | en_US |
dc.identifier.spage | 114 | en_US |
dc.identifier.epage | 118 | en_US |
dc.identifier.volume | 97 | en_US |
dc.identifier.doi | 10.1016/j.elecom.2018.11.004 | en_US |
dcterms.abstract | In this work, we propose a novel energy-transfer-based photoelectrochemical (PEC) platform for probing of protein-protein interaction, which associates intimately with zinc-dependent cleavage and substrate specificities in the enzymatic activities of botulinum neurotoxin (BoNT). Specifically, by using substrate protein SNAP-25 as the energy-transfer nanoprobe, an exciton-plasmon interaction (EPI) based strategy between CdS quantum dots (QDs) and Au nanoparticles (NPs) in a PEC system is constructed with the photocurrent declining. Interestingly, the EPI effect is then interrupted by the target botulinum neurotoxin serotype A light chain (BoNT-LCA) special cleavage of the probe SNAP-25, leading to the photocurrent recovery. Therefore, the enzymatic activity of BoNT-LCA could be sensitively detected with a detection limit of 1 pg/mL. Unlike conventional DNA-programable assembly, a protein probe is used to bridge the excitons and plasmons in this work, which provides a new route for the investigation of the EPI-based bioassay. | - |
dcterms.accessRights | open access | en_US |
dcterms.bibliographicCitation | Electrochemistry communications, 2018, v. 97, p. 114-118 | - |
dcterms.isPartOf | Electrochemistry communications | - |
dcterms.issued | 2018 | - |
dc.identifier.isi | WOS:000451326800025 | - |
dc.identifier.scopus | 2-s2.0-85056777729 | - |
dc.identifier.eissn | 1873-1902 | en_US |
dc.description.validate | 201902 bcma | en_US |
dc.description.oa | Version of Record | en_US |
dc.identifier.FolderNumber | OA_IR/PIRA | en_US |
dc.description.pubStatus | Published | en_US |
Appears in Collections: | Journal/Magazine Article |
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File | Description | Size | Format | |
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Lin_novel protein_binding_strategy.pdf | 1.75 MB | Adobe PDF | View/Open |
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